[NMR paper] Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.
Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.
J Biomol NMR. 2013 Jan 18;
Authors: Ghosh U, Xie L, Weliky DP
Abstract...
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[NMR paper] Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-eno
Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase.
Related Articles Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase.
J Biomol NMR. 2004 Jan;28(1):11-29
Authors: McDowell LM, Poliks B, Studelska DR, O'Connor RD, Beusen DD, Schaefer J
The 46-kD enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the condensation of shikimate-3-phosphate (S3P) and phosphoenolpyruvate to form EPSP....
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[NMR paper] Identification of residues involved in the interaction of Staphylococcus aureus fibro
Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the (4)F1(5)F1 module pair of human fibronectin using heteronuclear NMR spectroscopy.
Related Articles Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the (4)F1(5)F1 module pair of human fibronectin using heteronuclear NMR spectroscopy.
Biochemistry. 2000 Mar 21;39(11):2887-93
Authors: Penkett CJ, Dobson CM, Smith LJ, Bright JR, Pickford AR, Campbell ID, Potts JR
Many...
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11-18-2010 09:15 PM
[NMR paper] Closed form of liganded glutamine-binding protein by rotational-echo double-resonance
Closed form of liganded glutamine-binding protein by rotational-echo double-resonance NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Closed form of liganded glutamine-binding protein by rotational-echo double-resonance NMR.
Biochemistry. 1997 Aug 5;36(31):9405-8
Authors: Klug CA, Tasaki K, Tjandra N, Ho C, Schaefer J
Rotational-echo double-resonance NMR has been used to determine internuclear distances in the complex of glutamine-binding protein and its ligand, l-glutamine. The...
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[NMR paper] In situ analysis of peptidyl DOPA in mussel byssus using rotational-echo double-reson
In situ analysis of peptidyl DOPA in mussel byssus using rotational-echo double-resonance NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles In situ analysis of peptidyl DOPA in mussel byssus using rotational-echo double-resonance NMR.
Arch Biochem Biophys. 1996 Sep 1;333(1):221-4
Authors: Klug CA, Burzio LA, Waite JH, Schaefer J
Rotational-echo double-resonance (REDOR) 13C NMR spectra with 2H dephasing have been obtained from plaques and threads from the byssus of...
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[NMR paper] Two-dimensional, rotational-echo double-resonance NMR of cell culture metabolism.
Two-dimensional, rotational-echo double-resonance NMR of cell culture metabolism.
Related Articles Two-dimensional, rotational-echo double-resonance NMR of cell culture metabolism.
J Biol Chem. 1993 Oct 5;268(28):20768-71
Authors: McDowell LM, Cohen ER, Schaefer J
Two-dimensional, rotational-echo double-resonance 13C NMR, a new solid-state NMR technique, has been used to show that the relative fluxes of the labeled chemical bond of L-serine along four metabolic pathways (direct purine synthesis, direct glycine incorporation into protein,...
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[NMR paper] Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete se
Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Related Articles Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Biochemistry. 1991 Nov 19;30(46):11186-92
Authors: Kalbitzer HR, Neidig KP, Hengstenberg W
Complete sequence-specific assignments of the 1H NMR spectrum of HPr protein from Staphylococcus aureus were obtained by two-dimensional NMR methods. Important secondary structure...
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[NMR paper] Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete se
Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Related Articles Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure.
Biochemistry. 1991 Nov 19;30(46):11186-92
Authors: Kalbitzer HR, Neidig KP, Hengstenberg W
Complete sequence-specific assignments of the 1H NMR spectrum of HPr protein from Staphylococcus aureus were obtained by two-dimensional NMR methods. Important secondary structure...
Staphylococcus aureus PeptidoglycanStem Packing by Rotational-Echo Double Resonance NMR Spectroscopy
Linear Mode
